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KMID : 0364819910290020085
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Korean Journal of Microbiology
1991 Volume.29 No. 2 p.85 ~ p.91
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Characterization of β-1,4-D-Glucan Glucanohydrolase Purified from Trichoderma koningii
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Lim, Dae Sik/임대식
Jeong, Choon Soo/Kang, Sa Ouk/Hah, Yung Chil/정춘수/강사욱/하영칠
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Abstract
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1
fl-1,4-D-Glucan glucanohydrolase(EC 3.2.1.4;F-II-IV) purified from Trichoderma
koningii was identified as a glycoprotein containing 9% carbohydrate. Isoelectric point of the enzyme was estimated to be 4.9 and molecular weight was determined to be approximately 58,
000. The porducts of p-nitrophenyi-cellobioside (PNPG2) catalyzed by the enzyme were pnitrophenol(PNP) and p-nitrophenyl-glucoside(PNPG,). The Km value for PNPGZ was estimated
to be 0.97 mM in case of the holoside linkage and 10.4 mM in case of the aglycon linkage and their kcat values were 1.8X 1Os min-´ and 7.5X 10° min-´, respectively. The product of p
nitrophenyl cellotriose(PNPG3) was only PNPG,. The Km value for PNPG3 was 695 pM and
kcat was 1X101 min-´, which implicates that the enzyme have higher affinity and higher
hydrolysis rate toward PNPG3 than toward PNPGZ. The enzyme showed its optimal activity at
pH 4.0-4.5 and at 60C. The effect of gluconolactone on the activity toward PNPG2 showed competitive inhibition pattern but glucose and cellobiose did not. The enzyme contained a high content of acidic and hydroxylated amino acids in contrast to basic amino acids.
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